Research workbench
High resolution crystal structure of ftsy-ng domain of E. COLI bound to fragment 1
Analyse High resolution crystal structure of ftsy-ng domain of E. COLI bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CVD
- Type
- protein
- Length
- 605 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10121
- Ligands
- 4ME, NA, NH4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 302 | — | P10121 |
| B | — | protein | 303 | — | P10121 |
Ligands and binding sites
- 4ME · methyl 1H-indole-4-carboxylate · ligand · 4 copies · chains A, B
- NA · Sodium ion · metal · chains B
- NH4 · Ammonium ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6CVD · High resolution crystal structure of FtsY-NG domain of E. coli bound to fragment 1 · the same entry in another collection · chain A against A, TM-score 1.00
- P10121 · AlphaFold monomer V2.0 prediction for signal recognition particle receptor ftsy (P10121) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P10121
- Elsewhere: RCSB PDB 6CVD · PDBe 6CVD · UniProt P10121
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